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Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division
To maintain cellular structure and integrity during division, Gram-negative bacteria must carefully coordinate constriction of a tripartite cell envelope of inner membrane, peptidoglycan (PG), and outer membrane (OM). It has remained enigmatic how this is accomplished. Here, we show that envelope ma...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4458516/ https://www.ncbi.nlm.nih.gov/pubmed/25951518 http://dx.doi.org/10.7554/eLife.07118 |
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author | Gray, Andrew N Egan, Alexander JF van't Veer, Inge L Verheul, Jolanda Colavin, Alexandre Koumoutsi, Alexandra Biboy, Jacob Altelaar, A F Maarten Damen, Mirjam J Huang, Kerwyn Casey Simorre, Jean-Pierre Breukink, Eefjan den Blaauwen, Tanneke Typas, Athanasios Gross, Carol A Vollmer, Waldemar |
author_facet | Gray, Andrew N Egan, Alexander JF van't Veer, Inge L Verheul, Jolanda Colavin, Alexandre Koumoutsi, Alexandra Biboy, Jacob Altelaar, A F Maarten Damen, Mirjam J Huang, Kerwyn Casey Simorre, Jean-Pierre Breukink, Eefjan den Blaauwen, Tanneke Typas, Athanasios Gross, Carol A Vollmer, Waldemar |
author_sort | Gray, Andrew N |
collection | PubMed |
description | To maintain cellular structure and integrity during division, Gram-negative bacteria must carefully coordinate constriction of a tripartite cell envelope of inner membrane, peptidoglycan (PG), and outer membrane (OM). It has remained enigmatic how this is accomplished. Here, we show that envelope machines facilitating septal PG synthesis (PBP1B-LpoB complex) and OM constriction (Tol system) are physically and functionally coordinated via YbgF, renamed CpoB (Coordinator of PG synthesis and OM constriction, associated with PBP1B). CpoB localizes to the septum concurrent with PBP1B-LpoB and Tol at the onset of constriction, interacts with both complexes, and regulates PBP1B activity in response to Tol energy state. This coordination links PG synthesis with OM invagination and imparts a unique mode of bifunctional PG synthase regulation by selectively modulating PBP1B cross-linking activity. Coordination of the PBP1B and Tol machines by CpoB contributes to effective PBP1B function in vivo and maintenance of cell envelope integrity during division. DOI: http://dx.doi.org/10.7554/eLife.07118.001 |
format | Online Article Text |
id | pubmed-4458516 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-44585162015-06-10 Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division Gray, Andrew N Egan, Alexander JF van't Veer, Inge L Verheul, Jolanda Colavin, Alexandre Koumoutsi, Alexandra Biboy, Jacob Altelaar, A F Maarten Damen, Mirjam J Huang, Kerwyn Casey Simorre, Jean-Pierre Breukink, Eefjan den Blaauwen, Tanneke Typas, Athanasios Gross, Carol A Vollmer, Waldemar eLife Microbiology and Infectious Disease To maintain cellular structure and integrity during division, Gram-negative bacteria must carefully coordinate constriction of a tripartite cell envelope of inner membrane, peptidoglycan (PG), and outer membrane (OM). It has remained enigmatic how this is accomplished. Here, we show that envelope machines facilitating septal PG synthesis (PBP1B-LpoB complex) and OM constriction (Tol system) are physically and functionally coordinated via YbgF, renamed CpoB (Coordinator of PG synthesis and OM constriction, associated with PBP1B). CpoB localizes to the septum concurrent with PBP1B-LpoB and Tol at the onset of constriction, interacts with both complexes, and regulates PBP1B activity in response to Tol energy state. This coordination links PG synthesis with OM invagination and imparts a unique mode of bifunctional PG synthase regulation by selectively modulating PBP1B cross-linking activity. Coordination of the PBP1B and Tol machines by CpoB contributes to effective PBP1B function in vivo and maintenance of cell envelope integrity during division. DOI: http://dx.doi.org/10.7554/eLife.07118.001 eLife Sciences Publications, Ltd 2015-05-07 /pmc/articles/PMC4458516/ /pubmed/25951518 http://dx.doi.org/10.7554/eLife.07118 Text en © 2015, Gray et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Microbiology and Infectious Disease Gray, Andrew N Egan, Alexander JF van't Veer, Inge L Verheul, Jolanda Colavin, Alexandre Koumoutsi, Alexandra Biboy, Jacob Altelaar, A F Maarten Damen, Mirjam J Huang, Kerwyn Casey Simorre, Jean-Pierre Breukink, Eefjan den Blaauwen, Tanneke Typas, Athanasios Gross, Carol A Vollmer, Waldemar Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division |
title | Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division |
title_full | Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division |
title_fullStr | Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division |
title_full_unstemmed | Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division |
title_short | Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division |
title_sort | coordination of peptidoglycan synthesis and outer membrane constriction during escherichia coli cell division |
topic | Microbiology and Infectious Disease |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4458516/ https://www.ncbi.nlm.nih.gov/pubmed/25951518 http://dx.doi.org/10.7554/eLife.07118 |
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